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Unreviewed, UniProtKB/TrEMBL Q9RHW0 (Q9RHW0_BACSP)

Last modified November 3, 2009. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · Ontologies · Sequences · References · Cross-references · Entry information

Names and origin

Protein namesSubmitted name:
    Pectate lyase EMBL BAA87892.1
OrganismBacillus sp. EMBL BAA87892.1
Taxonomic identifier1409 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

Ontologies

Keywords
   Molecular functionLyase EMBL BAA87892.1
Gene Ontology (GO)
   Cellular componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular functionpectate lyase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
Q9RHW0-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 99D04821B09DE523

FASTA22423,751
        10         20         30         40         50         60 
MKKLLGLILS AALTLSLYGL EPQVAEAAPT VVHETIRVPA GQTFDGKGQT YVANPNTLGD 

        70         80         90        100        110        120 
GSQAENQKPI FRLEAGASLK NVVIGAPAAD GVHCYGDCTI TNVIWEDVGE DALTLKSSGT 

       130        140        150        160        170        180 
VNISGGAAYK AYDKVFQINA AGTINIRNFR ADDIGKLVRQ NGGTTYKVVM NVENCNISRV 

       190        200        210        220 
KDAILRTDSS TSTGRIVNTR YSNVPTLFKG FKSGNTTASG NTQY 

« Hide

References

[1]"Deduced amino-acid sequence and possible catalytic residues of a novel pectate lyase from an alkaliphilic strain of Bacillus."
Hatada Y., Saito K., Koike K., Yoshimatsu T., Ozawa T., Kobayashi T., Ito S.
Eur. J. Biochem. 267:2268-2275(2000) [PubMed: 10759850] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: KSM-P15 EMBL BAA87892.1.
[2]"Crystallization and preliminary X-ray analysis of high-alkaline pectate lyase."
Akita M., Suzuki A., Kobayashi T., Ito S., Yamane T.
Acta Crystallogr. D Biol. Crystallogr. 56:749-750(2000) [PubMed: 10818352] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 28-224.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB011839 Genomic DNA. Translation: BAA87892.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EE6X-ray2.30A28-224[»]
ModBaseSearch...

Protein family/group databases

CAZyPL3. Polysaccharide Lyase Family 3.

Enzyme and pathway databases

BRENDA4.2.2.2. 1000.

Family and domain databases

InterProIPR004898. Pectate_lyase_cat.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PfamPF03211. Pectate_lyase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ9RHW0_BACSP
AccessionPrimary (citable) accession number: Q9RHW0
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: November 3, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
Names and origin · Protein attributes · Ontologies · Sequences · References · Cross-references · Entry information